Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The soybean cultivar BR 36 with conventional levels of trypsin inhibitors activity and the soybean line BRM95-5262, which was genetically selected to contain low activity of trypsin inhibitors were used for biological assays with rats. BR 36 and BRM95-5262 contained 40 and 20, and 30 and 20% of relative residual activity of trypsin inhibitors, respectively. The mean values of PER and NPR showed that treatments with crude soybeans were minor than treatments with soybean thermically processed. However, the treatments of thermically processed soybean did not showed significative differences (p > or = 0.05). When the trypsin inhibitors activity were 8.61 and 8.44 UIT/mg of samples or 20 and 30% of relative residual activity of cultivar BR 36 and line BRM95-5262, respectively, it was observed that mean values of PER and NPR were not significatives. The mean values of CDA and CDV of treatments with crude soybeans were minor than treatment with casein and similar to the treatments with soybean thermically processed. So, it can be concluded that the biological evaluation obtained with soybean protein were dependent of initial trypsin inhibitors activities and of its respective thermical treatment. There was advantage in the use of BRM95-5262 soybean line with low trypsin inhibitors activity.
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PMID:[Biological evaluation of soybean line with low trypsin inhibitor activities]. 1167 52

Molecular dynamics (MD) simulations followed by molecular mechanics generalized Born surface area (MM-GBSA) analyses have been carried out to study the selectivity of two neutral and weakly basic P1 group inhibitors (177 and CDA) to thrombin and trypsin. Detailed binding free energies between these inhibitors and individual protein residues are calculated by using a per-residue basis decomposition method. The analysis of the detailed interaction energies provides insight on the protein-inhibitor-binding mechanism and helps to elucidate the basis for achieving selectivity through interpretation of the structural and energetic results from the simulations. The study shows that the dominant factor of selectivity for both inhibitors is van der Waals energy, which suggests better shape complementarity and packing with thrombin. Nonpolar solvation free energy and total entropy contribution are also in favor of selectivity, but the contributions are much smaller. Binding mode and structural analysis show that 177 binds to thrombin and trypsin in a similar binding mode. In contrast, the CDA binds to thrombin and trypsin in very different modes.
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PMID:Selectivity of neutral/weakly basic P1 group inhibitors of thrombin and trypsin by a molecular dynamics study. 1868 Jan 36

An elevated serum tryptase concentration is considered a specific marker for systemic mast cell activation, a central feature of anaphylaxis. However, in some cases of acute cardiovascular death, high concentrations of serum tryptase are also observed. We compared the postmortem serum tryptase concentrations in 74 cases assigned to the following four groups: anaphylactic deaths (Group A, n = 20), acute cardiac deaths (Group ACD, n = 30), acute dissecting aneurysm ruptures (Group ADA, n = 10), and controls (Group C, n = 14). Additionally, the cutoff between Group A and the other groups was calculated using receiver-operating characteristic (ROC) curve analysis. Tryptase concentrations were markedly elevated in Group A (p < 0.001), Group ACD (p = 0.015), and Group ADA (p = 0.005). The optimal cutoff was 43 ng/mL, the sensitivity was 90%, and the specificity was 98%. While elevated concentrations of tryptase were noted in practical autopsy cases, due attention should be paid to the differential diagnosis between anaphylactic and acute cardiovascular deaths.
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PMID:Postmortem Serum Tryptase Levels with Special Regard to Acute Cardiac Deaths. 2816 90